Refined solution structure of calmodulin N-terminal domain. Determined by solution NMR. Released 22 Sept 2000.
Explore 1F70 in 3D Show helices and sheets RCSB PDB PDBe
1F70 contains 6 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| α-helix | 6-18 | 13 | |
| β-strand | 26-28 | 3 | 1 |
| α-helix | 29-31 | 3 | |
| α-helix | 32-39 | 8 | |
| α-helix | 45-55 | 11 | |
| β-strand | 62-64 | 3 | 1 |
| α-helix | 65-75 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin | A | protein | 76 | Xenopus laevis | P0DP33 (AlphaFold model) |
>1F70_1 CALMODULIN (chains A) ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKM
Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings. Chou, J.J., Li, S., Bax, A. J Biomol NMR (2000) 18:217-227. DOI 10.1023/A:1026563923774 · PubMed
Other PDB entries of the same protein (UniProt P0DP33 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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